| |
|
|
|
Registro Completo |
|
Biblioteca(s): |
Embrapa Recursos Genéticos e Biotecnologia. |
|
Data corrente: |
15/02/2005 |
|
Data da última atualização: |
29/05/2018 |
|
Autoria: |
TIROLI, A. O.; TASIC, L.; OLIVEIRA, C. L. P.; BLOCH JUNIOR, C.; TORRIANI, I.; FARAH, C. S.; RAMOS, C. H. I. |
|
Título: |
Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras. |
|
Ano de publicação: |
2005 |
|
Fonte/Imprenta: |
The FEBS Journal, v. 272, n. 2, p. 779-790, 2005. |
|
Idioma: |
Inglês |
|
Conteúdo: |
The troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137. MenosThe troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. O... Mostrar Tudo |
|
Palavras-Chave: |
Muscle. |
|
Categoria do assunto: |
-- |
|
URL: |
https://ainfo.cnptia.embrapa.br/digital/bitstream/item/177877/1/ID-24788.pdf
|
|
Marc: |
LEADER 02317naa a2200205 a 4500
001 1185506
005 2018-05-29
008 2005 bl uuuu u00u1 u #d
100 1 $aTIROLI, A. O.
245 $aMapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras.$h[electronic resource]
260 $c2005
520 $aThe troponin (Tn) complex is formed by TnC, TnI and TnT and is responsible for the calcium-dependent inhibition of muscle contraction. TnC and TnI interact in an antiparallel fashion in which the N domain of TnC binds in a calcium-dependent manner to the C domain of TnI, releasing the inhibitory effect of the latter on the actomyosin interaction. While the crystal structure of the core cardiac muscle troponin complex has been determined, very little high resolution information is available regarding the skeletal muscle TnITnC complex. With the aim of obtaining structural information regarding specific contacts between skeletal muscle TnC and TnI regulatory domains, we have constructed two recombinant chimeric proteins composed of the residues 191 of TnC linked to residues 98182 or 98147 of TnI. The polypeptides were capable of binding to the thin filament in a calcium-dependent manner and to regulate the ATPase reaction of actomyosin. Small angle X-ray scattering results showed that these chimeras fold into compact structures in which the inhibitory plus the C domain of TnI, with the exception of residues 148182, were in close contact with the N-terminal domain of TnC. CD and fluorescence analysis were consistent with the view that the last residues of TnI (148182) are not well folded in the complex. MS analysis of fragments produced by limited trypsinolysis showed that the whole TnC N domain was resistant to proteolysis, both in the presence and in the absence of calcium. On the other hand the TnI inhibitory and C-terminal domains were completely digested by trypsin in the absence of calcium while the addition of calcium results in the protection of only residues 114137.
653 $aMuscle
700 1 $aTASIC, L.
700 1 $aOLIVEIRA, C. L. P.
700 1 $aBLOCH JUNIOR, C.
700 1 $aTORRIANI, I.
700 1 $aFARAH, C. S.
700 1 $aRAMOS, C. H. I.
773 $tThe FEBS Journal$gv. 272, n. 2, p. 779-790, 2005.
Download
Esconder MarcMostrar Marc Completo |
|
Registro original: |
Embrapa Recursos Genéticos e Biotecnologia (CENARGEN) |
|
|
Biblioteca |
ID |
Origem |
Tipo/Formato |
Classificação |
Cutter |
Registro |
Volume |
Status |
URL |
Voltar
|
|
|
| Registros recuperados : 13 | |
| 3. |  | FULAZ, S. F.; CABRINI, F. M.; BORRO, L.; TASIC, L.; NESHICH, G. Computational Biology tools in design of an agrochemical against Xylella fastidiosa. In: CONGRESS OF THE INTERNATIONAL UNION FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 23.; ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 44., 2015, Foz do Iguaçu. Biochemistry for a better world: abstracts book. [Foz do Iguaçu]: SBBq, 2015. p. 143. C.016.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
|    |
| 5. | | SANTOS, R. V. dos; VILLALTA-ROMERO, F.; STANISIC, D.; BORRO, L.; NESHICH, G.; TASIC, L. Citrus bioflavonoid, hesperetin, as inhibitor of two thrombin-like snake venom serine proteases isolated from Crotalus simus. Toxicon, v. 143, p. 36-43, Mar. 2018.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
|  |
| 6. | | SCHULTZ, L. G.; VILLALTAROMERO, F.; BORRO, L.; JARDINE, J. G.; NESHICH, G.; TASIC, L. The host/guest interactions of the key protein for the bipolar disorder. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 45., 2016, Natal. Livro de resumos... [Natal]: Sociedade Brasileira de Bioquímica e Biologia Molecular, 2016. Não paginado. Na publicação: José Jardine.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
| |
| 7. | | VILLALTA-ROMERO, F.; BORRO, l.; MANDIC, B.; ESCALANTE, T.; RUCAVADO, A.; GUTIÉRREZ, J. M.; NESHICH, G.; TASIC, L. Discovery of small molecule inhibitors for the snake venom metalloprotease BaP1 using in silico and in vitro tests. Bioorganic & Medicinal Chemistry Letters, v. 27, p. 2018-2022, 2017.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
| |
| 8. | | FULAZ, S. F.; CABRINI, F. M.; CARVALHO, D. J. P.; BORRO, L. C.; SANTOS, C. A. dos; BELOTI, L. L.; NESHICH, G.; SOUZA, A. P. de; TASIC, L. Design of inhibitors for the PilT protein from Xylella fastidiosa using in silico and in vitro approaches. In: ANNUAL MEETING OF THE BRAZILIAN SOCIETY FOR BIOCHEMISTRY AND MOLECULAR BIOLOGY, 45., 2016, Natal. Livro de resumos... [Natal]: Sociedade Brasileira de Bioquímica e Biologia Molecular, 2016. Não paginado.| Tipo: Resumo em Anais de Congresso |
| Biblioteca(s): Embrapa Agricultura Digital. |
| |
| 9. | | MASCARIN, G. M.; MARINHO-PRADO, J. S.; ASSALIN, M. R.; MARTINS, L. G.; BRAGA, E. S.; TASIC, L.; DITA RODRIGUES, M. A.; LOPES, R. B. Natural occurrence of Beauveria caledonica, pathogenicity to Cosmopolites sordidus and antifungal activity against Fusarium oxysporum f. sp. cubense. Pest Management Science, v. 78, n. 11, p. 4458-4470, 2022.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Meio Ambiente; Embrapa Recursos Genéticos e Biotecnologia. |
| |
| 10. | | TIROLI, A. O.; TASIC, L.; OLIVEIRA, C. L. P.; BLOCH JUNIOR, C.; TORRIANI, I.; FARAH, C. S.; RAMOS, C. H. I. Mapping contacts between regulatory domains of skeletal muscle TnC and Tnl by analyses of a single-chain chimeras. The FEBS Journal, v. 272, n. 2, p. 779-790, 2005.| Biblioteca(s): Embrapa Recursos Genéticos e Biotecnologia. |
| |
| 11. | | ASSALIN, M. R.; SOUZA, D. R. C. de; ROSA, M. A.; MOLTOCARO, R. C. R.; CASTANHA, R. F.; VILELA, E. S. D.; TASIC, L.; DURÁN, N. Thiamethoxam used as nanopesticide for the effective management of Diaphorina citri psyllid: an environmental-friendly formulation. International Journal of Pest Management, p.1-9, 2022. Online first.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 4 |
| Biblioteca(s): Embrapa Meio Ambiente. |
| |
| 12. | | RODRIGUES, A. G.; PING, L. Y.; MARCATO, P. D.; ALVES, O. L.; SILVA, M. C. P.; RUIZ, R. C.; MELO, I. S. de; TASIC, L.; SOUZA, A. O. de. Biogenic antimicrobial silver nanoparticles produced by fungi. Applied Microbiology and Biotechnology, New York, v. 97, p. 775-782, 2013.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 1 |
| Biblioteca(s): Embrapa Meio Ambiente. |
| |
| 13. | | NESHICH, I. A. P.; NISHIMURA, L.; MORAES, F. R. de; SALIM, J. A.; VILLALTA-ROMERO, F.; BORRO, L.; YANO, I. H.; MAZONI, I.; TASIC, L.; JARDINE, J. G.; NESHICH, G. Computational Biology tools for identifying specific ligand binding residues for novel agrochemical and drug design. Current Protein and Peptide Science, v. 16, n. 8, p. 701-717, 2015.| Tipo: Artigo em Periódico Indexado | Circulação/Nível: A - 2 |
| Biblioteca(s): Embrapa Agricultura Digital. |
| |
| Registros recuperados : 13 | |
|
| Nenhum registro encontrado para a expressão de busca informada. |
|
|
